Any feedback?
Information on EC 2.7.7.48 - RNA-directed RNA polymerase and Organism(s) Influenza A virus and UniProt Accession P31343
for references in articles please use BRENDA:EC2.7.7.48Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.7.48 RNA-directed RNA polymeraseIUBMB Comments
Catalyses RNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. See also EC 2.7.7.6 DNA-directed RNA polymerase.
Specify your search results
Word Map
- 2.7.7.48
- viruses
- strand
-
rnaps
-
single-stranded
- bacteriophage
- chromatin
- vaccine
- infectious
-
holoenzyme
- rrna
- helicase
- dsrnas
- ribonucleoproteins
- virion
- coronavirus
-
dna-dependent
-
outbreak
- replicons
- covid-19
- polyproteins
-
footprint
-
polyadenylation
- fever
- dengue
- pandemic
- polya
- nucleocapsids
-
serotype
- ribavirin
-
sequence-specific
- pre-mrnas
-
virological
-
non-structural
- duplex
-
stem-loops
- nucleoprotein
-
virus-infected
-
supercoiled
- rifampicin
-
unwind
-
virus-like
-
nucleolar
-
non-nucleoside
- gastroenteritis
- encephalitis
-
stall
-
anti-hcv
- dicer
-
virus-specific
- rotavirus
- synthesis
- drug development
- pharmacology
- medicine
- analysis
- molecular biology
The taxonomic range for the selected organisms is: Influenza A virus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
rna polymerase, rna-binding protein, rna-dependent rna polymerase, rdrp, nonstructural protein, transcriptase, vp1 protein, pol iv, rna-dependent rna polymerases, ns5b polymerase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
111 kDa protein
-
-
-
-
180 kDa protein
-
-
-
-
182 kDa protein
-
-
-
-
183 kDa protein
-
-
-
-
186 kDa protein
-
-
-
-
216.5 kDa protein
-
-
-
-
2A protein
-
-
-
-
3D pol
-
-
-
-
3D polymerase
-
-
-
-
69.6 kDa protein
-
-
-
-
core protein
-
-
-
-
core protein VP1
-
-
-
-
inner layer protein VP1
-
-
-
-
L protein
-
-
-
-
large structural protein
-
-
-
-
M1 phosphoprotein
-
-
-
-
NIB
-
-
-
-
nonstructural phosphoprotein
-
-
-
-
nonstructural protein
-
-
-
-
nonstructural protein 5B
-
-
-
-
NS5B
-
-
-
-
NS5B protein
-
-
-
-
nucleocapsid phosphoprotein
-
-
-
-
nucleotidyltransferase, ribonucleate, RNA-dependent
-
-
-
-
ORF1
-
-
-
-
ORF1A
-
-
-
-
ORF1B
-
-
-
-
P protein
-
-
-
-
P180
-
-
-
-
P3D
-
-
-
-
P66
-
-
-
-
P70
-
-
-
-
P88 protein
-
-
-
-
PB1
-
-
-
-
PB1 proteins
-
-
-
-
PB2
-
-
-
-
PB2 proteins
-
-
-
-
Phage f2 replicase
-
-
-
-
Pol
-
-
-
-
polymerase acidic protein
-
-
-
-
polymerase basic 1 protein
-
-
-
-
polymerase L
-
-
-
-
proteins PB1
-
-
-
-
proteins, PB 2
-
-
-
-
proteins, specific or class, lambda3, of reovirus
-
-
-
-
proteins, specific or class, PB 1
-
-
-
-
proteins, specific or class, PB 2
-
-
-
-
Q-beta replicase
-
-
-
-
Qbeta replicase
-
-
-
-
Qbeta-replicase
-
-
-
-
RDRP
replicase, phage f2
-
-
-
-
replicase, Qbeta
-
-
-
-
ribonucleic acid replicase
-
-
-
-
ribonucleic acid-dependent ribonucleate nucleotidyltransferase
-
-
-
-
ribonucleic acid-dependent ribonucleic acid polymerase
-
-
-
-
ribonucleic replicase
-
-
-
-
ribonucleic synthetase
-
-
-
-
RNA nucleotidyltransferase (RNA-directed)
-
-
-
-
RNA polymerase
RNA replicase
-
-
-
-
RNA synthetase
-
-
-
-
RNA transcriptase
-
-
-
-
RNA-binding protein
-
-
-
-
RNA-dependent ribonucleate nucleotidyltransferase
-
-
-
-
RNA-dependent RNA polymerase
RNA-dependent RNA replicase
-
-
-
-
RNA-directed RNA polymerase
-
-
-
-
sigma NS protein
-
-
-
-
transcriptase
-
-
-
-
VP1
-
-
-
-
VP1 protein
-
-
-
-
RDRP
-
-
-
-
RNA-dependent RNA polymerase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside-triphosphate:RNA nucleotidyltransferase (RNA-directed)
Catalyses RNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. See also EC 2.7.7.6 DNA-directed RNA polymerase.
CAS REGISTRY NUMBER
COMMENTARY
9026-28-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
various RNA substrates: Alu RNA, 110 nucleotides of the Alu domain of Pyrococcus horikoshii SRP RNA, Candida albicans tRNAAsn, U-rich RNA (59-GGCCAUCCUGU7 CCCU11CU19-39)29, ph-RNA of 81 nucleotides30, and short ph-RNA of 36 nucleotides comprising just the conserved 3' and 5' ends with a short linker and circular single stranded DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in vitro transcription using the model RNA template, v84
-
-
?
additional information
?
-
the polymerase protein also harbors an intrinsic RNA and DNA endonuclease activity that cleaves host mRNAs during cap-snatching, inhibited by 2,4-dioxo-4-phenylbutanoic and activated by Mn2+, with the amino-terminal 209 residues of the PA subunit containing the endonuclease active site, structure-function analysis, overview
-
-
?
additional information
?
-
-
the RNA polymerase complex consists of three subunits, PB1, PB2, and PA. These polymerase subunits and nucleoprotein, together with the viral RNA, form the viral ribonucleoprotein complex, which is the minimum component for viral RNA replication and transcription
-
-
?
additional information
?
-
-
the heterotrimeric complex of PB1, PB2 and PA subunits cooperate in the transcription and replication of the viral genome, the N-terminal region of the PA subunit of two recent H5N1 strains can influence promoter binding and RNA polymerase activity as well as virulence of the strains, overview
-
-
?
additional information
?
-
-
the RdRp catalyzes all the biochemical reactions of influenza virus transcription and replication in vitro, dinucleotide ApG and globin mRNA-primed transcription, de novo initiation/replication, and polyadenylation
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the RNA polymerase complex consists of three subunits, PB1, PB2, and PA. These polymerase subunits and nucleoprotein, together with the viral RNA, form the viral ribonucleoprotein complex, which is the minimum component for viral RNA replication and transcription
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
activates optimally at 8 mM, recombinant viral enzyme purified from insect cells
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
inhibition of the assembly of the viral nucleoprotein, by RuvB-like protein 2, RBL2, and subsequent inhibition of the formation of the viral ribonucleoprotein complex inhibits viral RNA replication, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
RanBP5
-
a member of importin beta family, required for PB1/PA heterodimer import into the nucleus, where the active heterotrimer of the enzyme is formed
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic analysis of the recombinant enzyme complex
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
strains A/WSN/33, H1N1, and A/NT/60/68, H3N2, show standard RNA polymerase activity, while strains A/HongKong/156/97, H5N1, and A/Vietnam/1194/04, H5N1, show increased polymerase activity correlated with enhanced promoter binding. The N-terminal region of the PA subunit is the major determinant of this enhanced promoter activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 42
-
28.7% at 4°C and 13.4% at 42°C of the activity at 25°C, no activity at 0°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
efficient polymerase assembly is a limiting factor in the viability of reassortant viruses, mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, overview. PB1 and PA form a dimer in the cytoplasm, which is imported into the nucleus, separately from PB2. The PB1/PA heterodimer is imported into the nucleus by RanBP5, a member of importin beta family. Once in the nucleus, the PB1/PA dimer associates with PB2 to form the trimeric polymerase
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is responsible for replication and transcription of the eight separate segments of the viral RNA genome in the nuclei of infected cells
malfunction
-
impairing the nuclear import of PB2 by mutating its nuclear localization signal leads to abnormal formation of the trimeric polymerase in the cytoplasm
additional information
additional information
-
efficient polymerase assembly is a limiting factor in the viability of reassortant viruses, mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, overview
additional information
-
the RNA polymerase of influenza virus is a heterotrimeric complex of PB1, PB2 and PA subunits, which cooperate in the transcription and replication of the viral genome
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
trimer
-
mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, overview. PB1 and PA form a dimer in the cytoplasm, which is imported into the nucleus separately from PB2. Once in the nucleus, the PB1/PA dimer associates with PB2 to form the trimeric polymerase. The strong interface that can be formed between the N-terminal extremity of PB2 and the C-terminal extremity of PB1 is present only in the fully assembled trimeric polymerase
heterotrimer
-
the RNA polymerase complex consists of three subunits, PB1, PB2, and PA. These polymerase subunits and nucleoprotein, together with the viral RNA, form the viral ribonucleoprotein complex, which is the minimum component for viral RNA replication and transcription
heterotrimer
-
the RNA polymerase of influenza virus is a heterotrimeric complex of PB1, PB2 and PA subunits, which cooperate in the transcription and replication of the viral genome. The N-terminal region of the PA subunit of two recent H5N1 strains can influence promoter binding
heterotrimer
the three subunits, PB1, PB2 and PA, are all required for both transcription and replication, PB1 carries the polymerase active site, PB2 includes the capped-RNA recognition domain, and PA, whose C-terminal domain consists of 13 alpha-helices and 9 beta-strands, is involved in assembly of the functional complex. The subunit interface is important for viral replication, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, at 20°C by the hanging drop method using a protein solution of 5-10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl and 2.5 mM MnCl2 and a reservoir composition of 1.2 M Li2SO4, 100 mM MES, pH 6.0, 10 mM Mg acetate and 3% ethylene glycol
a large fragment of subunit PA bound to a fragment of subunit PB1, hanging dropn vapour diffusion method, 20°C, mixing of 0.001 ml of protein solution, containing 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 100 mM sodium chloride, and 0.001 ml of reservoir solution consisting of 100 mM Tris-HCl, pH 7.5, and 2.4 M sodium formate, X-ray diffraction structure determination and analysis at 2.3 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L640D
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
L666D
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
V636S
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
W706A
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
additional information
-
impairing the nuclear import of PB2 by mutating its nuclear localization signal leads to abnormal formation of the trimeric polymerase in the cytoplasm
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by affinity chromatography and gel filtration
recombinant His-tagged subunits PA and PB1 from Escherichia coli by nickel affinity chromatography
recombinant viral His18-tagged enzyme components from Sf21AE and TN5 insect cells
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of the viral His18-tagged enzyme components in Sf21AE and TN5 insect cells, establishing a single-round transcription system
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, S.; Weng, L.; Geng, L.; Wang, J.; Zhou, J.; Deubel, V.; Buchy, P.; Toyoda, T.
Biochemical and kinetic analysis of the influenza virus RNA polymerase purified from insect cells
Biochem. Biophys. Res. Commun.
391
570-574
2009
influenza A virus
Kakugawa, S.; Shimojima, M.; Neumann, G.; Goto, H.; Kawaoka, Y.
RuvB-like protein 2 is a suppressor of influenza A virus polymerases
J. Virol.
83
6429-6434
2009
influenza A virus
Huet, S.; Avilov, S.V.; Ferbitz, L.; Daigle, N.; Cusack, S.; Ellenberg, J.
Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy
J. Virol.
84
1254-1264
2010
influenza A virus
Obayashi, E.; Yoshida, H.; Kawai, F.; Shibayama, N.; Kawaguchi, A.; Nagata, K.; Tame, J.R.; Park, S.Y.
The structural basis for an essential subunit interaction in influenza virus RNA polymerase
Nature
454
1127-1131
2008
influenza A virus (P03433), influenza A virus
Dias, A.; Bouvier, D.; Crepin, T.; McCarthy, A.A.; Hart, D.J.; Baudin, F.; Cusack, S.; Ruigrok, R.W.
The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit
Nature
458
914-918
2009
influenza A virus (P31343), influenza A virus Victoria/3/1975 H3N2 (P31343)
EXTERNAL LINKS (specific for EC-Number 2.7.7.48)
Transporter Classification Database (TCDB): 1.G.3.1.7, 1.A.53.1.5, 1.A.85.1.6, 1.A.122.1.2, 1.A.53.1.7, 1.A.85.1.7, 1.G.3.1.2, 1.G.3.1.1, 1.A.85.1.4, 1.A.85.1.8, 1.A.53.1.11, 1.A.53.1.6, 1.A.85.1.1
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
